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Q01594

- ALLN1_ALLSA

UniProt

Q01594 - ALLN1_ALLSA

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Protein

Alliin lyase 1

Gene
N/A
Organism
Allium sativum (Garlic)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli

Functioni

Able to cleave the C-S bond of sulfoxide derivatives of Cys to produce allicin, thus giving rise to all sulfur compounds which are responsible for most of the properties of garlic, such as the specific smell and flavor as well as the health benefits like blood lipid or blood pressure lowering.

Catalytic activityi

An S-alkyl-L-cysteine S-oxide = an alkyl sulfenate + 2-aminoacrylate.

Cofactori

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Binding sitei132 – 1321Chloride
Binding sitei136 – 1361Chloride
Binding sitei138 – 1381Chloride

GO - Molecular functioni

  1. alliin lyase activity Source: UniProtKB-EC
  2. pyridoxal phosphate binding Source: InterPro
Complete GO annotation...

Keywords - Molecular functioni

Lyase

Keywords - Ligandi

Chloride, Pyridoxal phosphate

Enzyme and pathway databases

BioCyciMetaCyc:MONOMER-13504.

Names & Taxonomyi

Protein namesi
Recommended name:
Alliin lyase 1 (EC:4.4.1.4)
Short name:
Alliinase-1
Alternative name(s):
Cysteine sulphoxide lyase 1
OrganismiAllium sativum (Garlic)
Taxonomic identifieri4682 [NCBI]
Taxonomic lineageiEukaryotaViridiplantaeStreptophytaEmbryophytaTracheophytaSpermatophytaMagnoliophytaLiliopsidaAsparagalesAmaryllidaceaeAllioideaeAllieaeAllium

Subcellular locationi

GO - Cellular componenti

  1. vacuole Source: UniProtKB-KW
Complete GO annotation...

Keywords - Cellular componenti

Vacuole

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Signal peptidei1 – 2828Sequence AnalysisAdd
BLAST
Propeptidei29 – 38101 PublicationPRO_0000020677
Chaini39 – 486448Alliin lyase 1PRO_0000020678Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Glycosylationi57 – 571N-linked (GlcNAc...)Sequence Analysis
Disulfide bondi58 ↔ 77
Disulfide bondi79 ↔ 88
Disulfide bondi82 ↔ 95
Glycosylationi184 – 1841N-linked (GlcNAc...)
Glycosylationi229 – 2291N-linked (GlcNAc...)Sequence Analysis
Modified residuei289 – 2891N6-(pyridoxal phosphate)lysine
Glycosylationi366 – 3661N-linked (GlcNAc...)
Disulfide bondi406 ↔ 414

Keywords - PTMi

Disulfide bond, Glycoprotein

Expressioni

Tissue specificityi

Bulb and shoots.

Interactioni

Subunit structurei

Homodimer.1 Publication

Structurei

Secondary structure

1
486
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Helixi44 – 5411Combined sources
Helixi59 – 613Combined sources
Beta strandi83 – 853Combined sources
Helixi105 – 1073Combined sources
Helixi108 – 1114Combined sources
Helixi115 – 1184Combined sources
Beta strandi120 – 1223Combined sources
Turni124 – 1274Combined sources
Beta strandi129 – 1313Combined sources
Helixi141 – 15414Combined sources
Beta strandi163 – 1686Combined sources
Helixi169 – 18113Combined sources
Turni185 – 1873Combined sources
Beta strandi194 – 1985Combined sources
Helixi204 – 2129Combined sources
Beta strandi218 – 2236Combined sources
Helixi224 – 2274Combined sources
Helixi233 – 2353Combined sources
Beta strandi236 – 2438Combined sources
Turni245 – 2473Combined sources
Beta strandi259 – 2635Combined sources
Turni269 – 2713Combined sources
Beta strandi281 – 2866Combined sources
Helixi287 – 2904Combined sources
Helixi294 – 2963Combined sources
Beta strandi299 – 3035Combined sources
Helixi306 – 31914Combined sources
Beta strandi320 – 3223Combined sources
Helixi325 – 34521Combined sources
Helixi352 – 37120Combined sources
Beta strandi374 – 3785Combined sources
Beta strandi386 – 3883Combined sources
Turni389 – 3924Combined sources
Beta strandi393 – 3953Combined sources
Beta strandi400 – 4067Combined sources
Helixi409 – 4113Combined sources
Helixi414 – 4207Combined sources
Helixi428 – 4314Combined sources
Beta strandi437 – 4415Combined sources
Helixi446 – 46015Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1LK9X-ray1.53A/B39-486[»]
2HORX-ray1.60A39-465[»]
2HOXX-ray1.40A/B/C/D39-465[»]
ProteinModelPortaliQ01594.
SMRiQ01594. Positions 39-465.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiQ01594.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini51 – 9747EGF-like; atypicalAdd
BLAST

Domaini

The 6 Cys residues of the EGF-like domain are arranged in a disulfide pattern different from the one found in the canonical EGFs. The function of this domain is unclear. It may be a binding site for other proteins or the docking site for a putative alliinase receptor.

Sequence similaritiesi

Belongs to the alliinase family.Curated
Contains 1 EGF-like domain.Curated

Keywords - Domaini

EGF-like domain, Signal

Family and domain databases

Gene3Di2.10.25.30. 1 hit.
3.40.640.10. 1 hit.
3.90.1150.10. 1 hit.
InterProiIPR006948. Alliinase_C.
IPR006947. EGF_alliinase.
IPR015424. PyrdxlP-dep_Trfase.
IPR015421. PyrdxlP-dep_Trfase_major_sub1.
IPR015422. PyrdxlP-dep_Trfase_major_sub2.
[Graphical view]
PfamiPF04864. Alliinase_C. 1 hit.
PF04863. EGF_alliinase. 1 hit.
[Graphical view]
SUPFAMiSSF53383. SSF53383. 1 hit.
PROSITEiPS00022. EGF_1. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

Q01594-1 [UniParc]FASTAAdd to Basket

« Hide

        10         20         30         40         50
MVESYKKIGS CNKMPCLVIL TCIIMSNSLV NNNNMVQAKM TWTMKAAEEA
60 70 80 90 100
EAVANINCSE HGRAFLDGII SEGSPKCECN TCYTGPDCSE KIQGCSADVA
110 120 130 140 150
SGDGLFLEEY WKQHKEASAV LVSPWHRMSY FFNPVSNFIS FELEKTIKEL
160 170 180 190 200
HEVVGNAAAK DRYIVFGVGV TQLIHGLVIS LSPNMTATPD APESKVVAHA
210 220 230 240 250
PFYPVFREQT KYFNKKGYVW AGNAANYVNV SNPEQYIEMV TSPNNPEGLL
260 270 280 290 300
RHAVIKGCKS IYDMVYYWPH YTPIKYKADE DILLFTMSKF TGHSGSRFGW
310 320 330 340 350
ALIKDESVYN NLLNYMTKNT EGTPRETQLR SLKVLKEVVA MVKTQKGTMR
360 370 380 390 400
DLNTFGFKKL RERWVNITAL LDQSDRFSYQ ELPQSEYCNY FRRMRPPSPS
410 420 430 440 450
YAWVKCEWEE DKDCYQTFQN GRINTQNGVG FEASSRYVRL SLIKTQDDFD
460 470 480
QLMYYLKDMV KAKRKTPLIK QLFIDQTETA SRRPFI
Length:486
Mass (Da):55,639
Last modified:July 1, 1993 - v1
Checksum:iD7862E867AD74383
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
Z12622 mRNA. Translation: CAA78268.1.
PIRiS29302.

Cross-referencesi

Web resourcesi

Protein Spotlight

What's that smell? - Issue 39 of October 2003

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
Z12622 mRNA. Translation: CAA78268.1 .
PIRi S29302.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
Entry Method Resolution (Å) Chain Positions PDBsum
1LK9 X-ray 1.53 A/B 39-486 [» ]
2HOR X-ray 1.60 A 39-465 [» ]
2HOX X-ray 1.40 A/B/C/D 39-465 [» ]
ProteinModelPortali Q01594.
SMRi Q01594. Positions 39-465.
ModBasei Search...
MobiDBi Search...

Protocols and materials databases

Structural Biology Knowledgebase Search...

Enzyme and pathway databases

BioCyci MetaCyc:MONOMER-13504.

Miscellaneous databases

EvolutionaryTracei Q01594.

Family and domain databases

Gene3Di 2.10.25.30. 1 hit.
3.40.640.10. 1 hit.
3.90.1150.10. 1 hit.
InterProi IPR006948. Alliinase_C.
IPR006947. EGF_alliinase.
IPR015424. PyrdxlP-dep_Trfase.
IPR015421. PyrdxlP-dep_Trfase_major_sub1.
IPR015422. PyrdxlP-dep_Trfase_major_sub2.
[Graphical view ]
Pfami PF04864. Alliinase_C. 1 hit.
PF04863. EGF_alliinase. 1 hit.
[Graphical view ]
SUPFAMi SSF53383. SSF53383. 1 hit.
PROSITEi PS00022. EGF_1. 1 hit.
[Graphical view ]
ProtoNeti Search...

Publicationsi

  1. "Isolation and characterization of alliinase cDNA clones from garlic (Allium sativum L.) and related species."
    van Damme E.J.M., Smeets K., Torrekens S., van Leuven F., Peumans W.J.
    Eur. J. Biochem. 209:751-757(1992) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA], PROTEIN SEQUENCE OF 39-58.
    Tissue: Shoot.
  2. "Purification, characterization, and crystallization of alliinase from garlic."
    Kuettner E.B., Hilgenfeld R., Weiss M.S.
    Arch. Biochem. Biophys. 402:192-200(2002) [PubMed] [Europe PMC] [Abstract]
    Cited for: CHARACTERIZATION, CRYSTALLIZATION.
    Tissue: Bulb.
  3. "The active principle of garlic at atomic resolution."
    Kuettner E.B., Hilgenfeld R., Weiss M.S.
    J. Biol. Chem. 277:46402-46407(2002) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (1.53 ANGSTROMS) OF 39-465, SUBUNIT.
    Tissue: Bulb.

Entry informationi

Entry nameiALLN1_ALLSA
AccessioniPrimary (citable) accession number: Q01594
Entry historyi
Integrated into UniProtKB/Swiss-Prot: July 1, 1993
Last sequence update: July 1, 1993
Last modified: November 26, 2014
This is version 97 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programPlant Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

3D-structure, Direct protein sequencing

Documents

  1. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  2. Protein Spotlight
    Protein Spotlight articles and cited UniProtKB/Swiss-Prot entries
  3. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3